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The sorLA cytoplasmic domain interacts with GGA1 and ‐2 and defines minimum requirements for GGA binding
Author(s) -
Jacobsen Linda,
Madsen Peder,
Nielsen Morten S.,
Geraerts Wijnand P.M.,
Gliemann Jørgen,
Smit August B.,
Petersen Claus M.
Publication year - 2002
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(01)03299-9
Subject(s) - endosome , signal transducing adaptor protein , cytoplasm , receptor , golgi apparatus , microbiology and biotechnology , mannose , transport protein , protein targeting , biochemistry , phosphorylation , biology , chemistry , membrane protein , endoplasmic reticulum , membrane
We report that the Vps10p domain receptor sorLA binds the adaptor proteins GGA1 and ‐2, which take part in Golgi–endosome sorting. The GGAs bind with differential requirements via three critical residues in the C‐terminal segment of the sorLA cytoplasmic tail. Unlike in sortilin and the mannose 6‐phosphate receptors, the GGA‐binding segment in sorLA contains neither an acidic cluster nor a dileucine. Our results support the concept of sorLA as a potential sorting receptor and suggest that key residues in sorLA and sortilin conform to a new type of motif (Ψ–Ψ–X–X–∅) defining minimum requirements for GGA binding to cytoplasmic receptor domains.